ID A0A1H6UM45_9EURY Unreviewed; 746 AA.
AC A0A1H6UM45; A0A2H4PZ51;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Archaeal Lon protease {ECO:0000256|ARBA:ARBA00022016, ECO:0000256|RuleBase:RU369001};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU369001};
DE AltName: Full=ATP-dependent protease La homolog {ECO:0000256|RuleBase:RU369001};
GN ORFNames=SAMN05444271_11163 {ECO:0000313|EMBL:SEI90787.1};
OS Halohasta litchfieldiae.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halohasta.
OX NCBI_TaxID=1073996 {ECO:0000313|EMBL:SEI90787.1, ECO:0000313|Proteomes:UP000198888};
RN [1] {ECO:0000313|EMBL:SEI90787.1, ECO:0000313|Proteomes:UP000198888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22187 {ECO:0000313|EMBL:SEI90787.1,
RC ECO:0000313|Proteomes:UP000198888};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC degradation of mutant and abnormal proteins as well as certain short-
CC lived regulatory proteins. Degrades polypeptides processively.
CC {ECO:0000256|RuleBase:RU369001}.
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC {ECO:0000256|ARBA:ARBA00026070, ECO:0000256|RuleBase:RU369001}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|RuleBase:RU369001}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU369001}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. Archaeal LonB
CC subfamily. {ECO:0000256|ARBA:ARBA00009579,
CC ECO:0000256|RuleBase:RU369001}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU369001}.
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DR EMBL; FNYR01000011; SEI90787.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6UM45; -.
DR STRING; 1073996.SAMN05444271_11163; -.
DR OrthoDB; 64652at2157; -.
DR Proteomes; UP000198888; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR004663; Lon_arc.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR046843; LonB_AAA-LID.
DR InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008268; Peptidase_S16_AS.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR002078; Sigma_54_int.
DR NCBIfam; TIGR00764; lon_rel; 1.
DR PANTHER; PTHR10046:SF46; ARCHAEAL LON PROTEASE; 1.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF20436; LonB_AAA-LID; 1.
DR Pfam; PF01078; Mg_chelatase; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU369001};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU369001};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01122};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU369001};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU369001};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000198888};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU369001};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU369001}.
FT TRANSMEM 235..268
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU369001"
FT DOMAIN 535..713
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..112
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 620
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 663
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 746 AA; 80626 MW; 3975B0E6A75DBB63 CRC64;
MSNDTDTDDG PPDSGVNDEK PSTTDDQSVD NGHDDGQQLT EESAGDPVDD QQSADDEPSQ
PEAVLTDDEL FESGPSGGDS RSRANTPSET NDDDDPPSIE ELGSDVEVDA PIADDVDKDD
LLGGLLIDST EDVSIPERLV DQVIGQEHAR DVIIKAAKQR RHVMMIGSPG TGKSMLAKAM
TELLPKEELQ DVLIYHNPDD GNKPKVRTVP AGKGEQIVDA HKEEARKRNQ MRTFLMWIII
AVVLGYALII AGQILLGILA AGIIYLAFRY ASRGSDAMVP NLLVNNSDTT TAPFRDATGG
HAGALLGDVR HDPFQSGGME TPSHDRVEPG AIHKANKGVL FIDEINTLDI RSQQHLMTAI
QEGEFSITGQ SERSSGAMVQ TEPVPTDFIM IAAGNLDAME NMHPALRSRI KGYGYEVYME
DTIEDTPEMR RKYVRFVAQE VANDGRLPQF DDEAIEEIIL EARRRAGRKG HLTLKFRDLG
GLVRVAGDIA RAEDAEFTTR DHVLQAKERS RSIEQQLADE FIERRKDYEL QVSDGYQVGR
VNGLAVMGED SGIMLPVMAE VTPSQGPGQV IATGQLKEMA EESVQNVSAI IKKFSDQNLA
EKDVHIQFVQ TGQSGVDGDS ASITVATAVI SALEDVGVSQ NLAMTGSLSV RGDVLPVGGV
THKIEAAAKA GCKTVIIPKA NEQDVMIEDE YREMIEIIPV SHISEVLEVA LEGEGEKDSL
IARLKSITGS ALQDGNVAGP SSPSPQ
//
